Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress

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• 作者：Katoh ; Yumiko ; Fujimoto ; Mitsuaki ; Nakamura ; Kosuke ; Inouye ; Sachiye ; Sugahara ; Kazuma ; Izu ; Hanae ; et. al.
• 关键词：Aggresome ; Molecular chaperone ; Crystallin ; Heat shock protein ; Ubiquitin
• 刊名：FEBS Letters
• 出版年：2004
• 出版时间：May 7, 2004
• 年：2004
• 卷：565
• 期：1-3
• 页码：28-32
• 全文大小：320 K

文摘

Protein aggregates are oligomeric complexes of misfolded proteins, and serve as the seeds of inclusion bodies termed aggresomes in the cells. Heat shock proteins (Hsps) prevent misfolding and aggregate formation. Here, we found that only avian Hsp25 dominantly accumulated in the aggresomes induced by proteasome inhibition. Molecular cloning of chicken Hsp25 (cHsp25) revealed that it belongs to the Hsp30 family, which is a subfamily of the α-crystallin/small Hsp gene family. Unexpectedly, overexpression of cHsp25 into HeLa cells promoted inclusion formation whereas overexpression of mouse Hsp27 and its chicken homologue did not. These results suggest that cHsp25 acts differently from other small Hsps on protein aggregates.